Data/hora: 14/06/2024 06:57:33

Provedor de dados: 	56	
País: 	Brazil	
Título: 	A new brain metalloendopeptidase which degrades the Alzheimer ß-amyloid 1-40 peptide producing soluble fragments without neurotoxic effects	
Autores: 	Carvalho,K.M.; França,M.S.F.; Camarão,G.C.; Ruchon,A.F.	
Data: 	1997-10-01	
Ano: 	1997	
Palavras-chave: 	Brain metalloendopeptidase; Alzheimer ß-amyloid 1-40 peptide; Alzheimer's disease.	
Resumo: 	A new metalloendopeptidase was purified to apparent homogeneity from a homogenate of normal human brain using successive steps of chromatography on DEAE-Trisacryl, hydroxylapatite and Sephacryl S-200. The purified enzyme cleaved the Gly33-Leu34 bond of the 25-35 neurotoxic sequence of the Alzheimer ß-amyloid 1-40 peptide producing soluble fragments without neurotoxic effects. This enzyme activity was only inhibited by divalent cation chelators such as EDTA, EGTA and o-phenanthroline (1 mM) and was insensitive to phosphoramidon and captopril (1 µM concentration), specific inhibitors of neutral endopeptidase (EC 3.4.24.11) and angiotensin-converting enzyme (EC 3.4.15.1), respectively. The high affinity of this human brain endopeptidase for ß-amyloid 1-40 peptide (Km = 5 µM) suggests that it may play a physiological role in the degradation of this substance produced by normal cellular metabolism. It may also be hypothesized that the abnormal accumulation of the amyloid ß-protein in Alzheimer's disease may be initiated by a defect or an inactivation of this enzyme.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001000002	
Editor: 	Associação Brasileira de Divulgação Científica	
Relação: 	10.1590/S0100-879X1997001000002	
Formato: 	text/html	
Fonte: 	Brazilian Journal of Medical and Biological Research  v.30 n.10 1997	
Fonte: 	info:eu-repo/semantics/openAccess